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Literature summary for 1.1.1.337 extracted from

  • Graupner, M.; Xu, H.; White, R.H.
    Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea (2000), J. Bacteriol., 182, 3688-3692.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanocaldococcus jannaschii
expression in Escherichia coli Methanothermus fervidus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
3-sulfopyruvate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii
0.07
-
3-sulfopyruvate cosubstrate NADH, pH 8.0, 70°C Methanothermus fervidus
0.11
-
oxaloacetate cosubstrate NADH, pH 8.0, 70°C Methanothermus fervidus
0.13
-
oxaloacetate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii
0.21
-
3-sulfopyruvate cosubstrate NADPH, pH 8.0, 70°C Methanocaldococcus jannaschii
0.21
-
3-sulfopyruvate cosubstrate NADPH, pH 8.0, 70°C Methanothermus fervidus
0.95
-
oxaloacetate cosubstrate NADPH, pH 8.0, 70°C Methanothermus fervidus
1.9
-
2-oxoglutarate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii
5.32
-
oxaloacetate cosubstrate NADPH, pH 8.0, 70°C Methanocaldococcus jannaschii
15
-
1-oxo-1,3,4,6-hexanetetracarboxylate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58820
-
-
Methanothermus fervidus P16142
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R)-3-sulfolactate + NAD+
-
Methanocaldococcus jannaschii 3-sulfopyruvate + NADH + H+
-
r
(2R)-3-sulfolactate + NAD+
-
Methanothermus fervidus 3-sulfopyruvate + NADH + H+
-
r
(S)-2-hydroxyglutarate + NAD+
-
Methanocaldococcus jannaschii 2-oxoglutarate + NADH + H+
-
r
(S)-lactate + NAD+
-
Methanocaldococcus jannaschii pyruvate + NADH + H+
-
r
(S)-lactate + NAD+
-
Methanothermus fervidus pyruvate + NADH + H+
-
r
1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+
-
Methanocaldococcus jannaschii 1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+
-
r
3-sulfopyruvate + NADH + H+
-
Methanocaldococcus jannaschii (S)-3-sulfolactate + NAD+
-
r
3-sulfopyruvate + NADH + H+
-
Methanothermus fervidus (S)-3-sulfolactate + NAD+
-
r
additional information enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate Methanothermus fervidus ?
-
?
additional information enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate Methanocaldococcus jannaschii ?
-
?
oxaloacetate + NADH + H+
-
Methanocaldococcus jannaschii (S)-malate + NAD+
-
?
oxaloacetate + NADH + H+
-
Methanothermus fervidus (S)-malate + NAD+
-
?

Synonyms

Synonyms Comment Organism
MJ1425
-
Methanocaldococcus jannaschii
MJ1425
-
Methanothermus fervidus

Cofactor

Cofactor Comment Organism Structure
NADH
-
Methanothermus fervidus
NADH ratio vmax/Km for NADH is about 20fold greater than for NADPH Methanocaldococcus jannaschii
NADPH
-
Methanothermus fervidus
NADPH ratio vmax/Km for NADH is about 20fold greater than for NADPH Methanocaldococcus jannaschii

General Information

General Information Comment Organism
physiological function enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin Methanocaldococcus jannaschii
physiological function enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin Methanothermus fervidus